ID A0A0A2IZR1_PENEN Unreviewed; 800 AA.
AC A0A0A2IZR1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=cysteine--tRNA ligase {ECO:0000256|ARBA:ARBA00012832};
DE EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
GN ORFNames=PEX2_044050 {ECO:0000313|EMBL:KGO62882.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO62882.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO62882.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO62882.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO62882.1}.
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DR EMBL; JQFZ01000018; KGO62882.1; -; Genomic_DNA.
DR RefSeq; XP_016603382.1; XM_016741680.1.
DR AlphaFoldDB; A0A0A2IZR1; -.
DR STRING; 27334.A0A0A2IZR1; -.
DR GeneID; 27677099; -.
DR HOGENOM; CLU_013528_3_1_1; -.
DR OrthoDB; 2140072at2759; -.
DR PhylomeDB; A0A0A2IZR1; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00435; cysS; 1.
DR PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF09190; DALR_2; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KGO62882.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 43..484
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT DOMAIN 526..579
FT /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT /evidence="ECO:0000259|Pfam:PF09190"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 711..741
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 759..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 89180 MW; 9C62459D317DBCF4 CRC64;
MSSRQQPPWR QPASSPDVQL PPLKVWNSLT KSKTPFVPID PAGKKVVWYA CGPTVYDDAH
LGHARNYVST DIIRRIMRDY FKFDVNFVMN ITDVDDKIIL RARQQHLFNE FVAVNPTITS
EVLDTVKCAF VAYLKKNLPL LDSELPPSRY QDEVEKIYAT ILNGGALPGN EKAGDDEAKV
KMHIKTAASA AKVIAQAESR DGSSADPALF AESFYSSAQD LILPYLDALK GALVDANDHS
IFTKLTKRYE DRFIKDMRDL NVLDPTELTR VTEYGDDIAA FVDRIVKNKF GYATKDGSVY
FDINAFEAAG HPYARLEPWS RSDNKLAAEG EGSLASKTTE KRGASDFALW KSSKPGEPAW
SSTWGKGRPG WHIECSAMAS ARLGNQMDIH SGGIDLAFPH HDNELAQSEA YWHGDHGHDQ
WVNYFLHMGH LSIQGSKMSK SLKNFTTIRE ALDRKDWTPR SLRIVFLLGS WKDGVEITED
LVNTGSSWEE KVNNFFLKVK DPAALQSSGT DTTFATDLEA AKKAVDDQLC DSFNTAAAMA
SISELISKFN IVDKATVPSK DVHAAAQWVT YMVNIFGLNG TASADSTEIG WSGIEIPEEA
KPYLYPLSAM RDTLREAARS KAGISAKDIE AAVAKASAPQ EASESAKPYA ELFSNFRAKV
VSLESSDTIG KDILSLCDRV RDIDLFDVGI ALEDRENQPA LVRPVTQEML KAREEKEIRA
LQKQAEKLKK EQEALKKAEK GKLSHLEMFR TNEYSAWDDE GMPTRDTAGE EITKSRAKKL
RKDWERQKKA HEAWLATQAK
//
